ArticlePLoS pathogens2021
Phosphatidic acid-mediated binding and mammalian cell internalization of the Vibrio cholerae cytotoxin MakA.
Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
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- A bacterial toxin as a novel anti-cancer drug modulating the tumor-microenvironment.Cell death & disease · 2025Article
- HapA protease targets PAR-1/2 to modulate ERK signalling and reduce cancer cell viability.Cell death discovery · 2025Article
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Hemagglutinin Protease HapA Associated With Vibrio cholerae Outer Membrane Vesicles (OMVs) Disrupts Tight and Adherens Junctions.Journal of extracellular vesicles · 2025Article
- Shaker/Kv1 potassium channel SHK-1 protects against pathogen infection and oxidative stress in C. elegans.PLoS genetics · 2025Article
- Single-cell RNA-seq reveals a key role forFrontiers in microbiology · 2025Article
- Anchorage of bacterial effector at plasma membrane via selective phosphatidic acid binding to modulate host cell signaling.PLoS pathogens · 2024Article
- Bacillus cereus cytotoxin K triggers gasdermin D-dependent pyroptosis.Cell death discovery · 2022Article
- A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.Journal of bacteriology · 2022Article
- Article
- A tripartite cytolytic toxin formed byProceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio cholerae is a noninvasive intestinal pathogen extensively studied as the causative agent of the human disease cholera. Our recent work identified MakA as a potent virulence factor of V. cholerae in both Caenorhabditis elegans and zebrafish, prompting us to investigate the potential contribution of MakA to pathogenesis also in mammalian hosts. In this study, we demonstrate that the MakA protein could induce autophagy and cytotoxicity of target cells. In addition, we observed that phosphatidic acid (PA)-mediated MakA-binding to the host cell plasma membranes promoted macropinocytosis resulting in the formation of an endomembrane-rich aggregate and vacuolation in intoxicated cells that lead to induction of autophagy and dysfunction of intracellular organelles. Moreover, we functionally characterized the molecular basis of the MakA interaction with PA and identified that the N-terminal domain of MakA is required for its binding to PA and thereby for cell toxicity. Furthermore, we observed that the ΔmakA mutant outcompeted the wild-type V. cholerae strain A1552 in the adult mouse infection model. Based on the findings revealing mechanistic insights into the dynamic process of MakA-induced autophagy and cytotoxicity we discuss the potential role played by the MakA protein during late stages of cholera infection as an anti-colonization factor.
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